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SDS-Page (Recombinant HDAC6 (597-728, deleted mutant) protein gel. HDAC6 protein was run on an 8% SDS-PAGE gel and stained with Coomassie blue.)

HDAC6 recombinant protein

Recombinant HDAC6 (597-728, deleted mutant) protein

Gene Names
HDAC6; HD6; JM21
Purity
The recombinant protein is >80% pure by SDS-PAGE.
Synonyms
HDAC6; Recombinant HDAC6 (597-728; deleted mutant) protein; HD6; JM21; CPBHM; PPP1R90; HDAC6 recombinant protein
Ordering
For Research Use Only!
Host
Baculovirus
Purity/Purification
The recombinant protein is >80% pure by SDS-PAGE.
Form/Format
Recombinant HDAC6 (597-728, deleted mutant) is supplied in 25mM Hepes pH7.5, 300mM NaCl, 5% Glycerol, 0.04% Triton X-100, 0.2mM TCEP, 0.2mg/ml 3× DYKDDDDK peptide.
Protein Species
Human
Tag
DYKDDDDK-Tag, His-Tag
Notes
Recombinant HDAC6 (597-728, deleted mutant) protein is suitable for the study of enzyme kinetics, screening inhibitors, and selectivity profiling. HDAC Activity Assay Conditions: 3uM H3K9ac (1-21) peptides was incubated with different concentrations of HDAC6 (597-728, deleted mutant) in 25mM Tris-HCl, pH 8.0, 137mM NaCl, 2.7mM KCl, 1mM MgCl2, 0.1mg/ml BSA for 30 minutes at 37 degree C followed by developing for 30 minutes at room temperature.
Dry Ice Shipment
Extra charge fee may add to your shipping cost as dry ice is required to ship this product.
Preparation and Storage
Recombinant proteins in solution are temperature sensitive and must be stored at -80 degree C to prevent degradation. Avoid repeated freeze/thaw cycles and keep on ice when not in storage.
Shipping Temp: Dry Ice

SDS-Page

(Recombinant HDAC6 (597-728, deleted mutant) protein gel. HDAC6 protein was run on an 8% SDS-PAGE gel and stained with Coomassie blue.)

SDS-Page (Recombinant HDAC6 (597-728, deleted mutant) protein gel. HDAC6 protein was run on an 8% SDS-PAGE gel and stained with Coomassie blue.)

Testing Data

(Recombinant HDAC6 (597-728, deleted mutant) protein activity assay. 3 ?M H3K9ac (1-21) peptides was incubated with different concentrations of HDAC6 (597-728, deleted mutant) in reaction buffer for 30 minutes at 37 degree C followed by developing for 30 minutes at room temperature.)

Testing Data (Recombinant HDAC6 (597-728, deleted mutant) protein activity assay. 3 ?M H3K9ac (1-21) peptides was incubated with different concentrations of HDAC6 (597-728, deleted mutant) in reaction buffer for 30 minutes at 37 degree C followed by developing for 30 minutes at room temperature.)
Related Product Information for HDAC6 recombinant protein
Short Description: Recombinant HDAC6 (597-728, deleted mutant) deletes the second catalytic domain. This recombinant protein was expressed in a baculovirus expression system (accession number NP_006035.2) with an N-terminal 6xHis-tag and DYKDDDDK-Tag. The molecular weight of the protein is 122.1 kDa. The recombinant protein is >80% pure by SDS-PAGE. It is suitable for use in histone deacetylase (HDAC) assays, in the study of enzyme kinetics, inhibitor screening, and selectivity profiling.

Background: HDAC6 (Histone Deacetylase 6) is a member of the class IIb mammalian histone deacetylases (HDACs) involved in regulating chromatin structure during transcription. These enzymes catalyze the removal of acetyl groups from lysine residues of histones or many cellular proteins. Lysine N-epsilon-acetylation is a dynamic, reversible and tightly regulatedprotein and histone modification that plays a major role in regulation of gene expression in various cellular functions. It consists of the transfer of an acetyl moiety from an acetyl coenzyme A to the e-amino group of a lysine residue. In vivo, acetylation is controlled by the antagonistic activities of histone acetyltransferases (HATs) and histone deacetylases (HDACs). The HDACs are grouped into four classes, on the basis of similarity to yeast counterparts: HDAC class I (HDAC1, HDAC2, HDAC3 and HDAC8), class II (HDAC4, HDAC5, HDAC6, HDAC7, 9 and 10), class III (SIRT1-7) and class IV (HDAC11). HDAC6 is a unique enzyme that harbors a full duplication of its deacetylase homology region, which appears to contribute independently to the overall activity of HDAC6 protein. Alpha-tubulin and HSP90 are two known substrates of HDAC6, playing an important role in cellular mechanisms related to the microtubule network and HSP90-dependent events. HDAC6 also participates in regulating expression of a group of genes involved in the remodeling of chromatin during cell differentiation.
Product Categories/Family for HDAC6 recombinant protein

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
131,419 Da
NCBI Official Full Name
histone deacetylase 6
NCBI Official Synonym Full Names
histone deacetylase 6
NCBI Official Symbol
HDAC6
NCBI Official Synonym Symbols
HD6; JM21
NCBI Protein Information
histone deacetylase 6
UniProt Protein Name
Histone deacetylase 6
UniProt Gene Name
HDAC6
UniProt Synonym Gene Names
KIAA0901; HD6
UniProt Entry Name
HDAC6_HUMAN

NCBI Description

Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene belongs to class II of the histone deacetylase/acuc/apha family. It contains an internal duplication of two catalytic domains which appear to function independently of each other. This protein possesses histone deacetylase activity and represses transcription. [provided by RefSeq, Jul 2008]

Uniprot Description

HDAC6: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Interacts with CBFA2T3, HDAC11 and SIRT2. Interacts with F-actin. Interacts with BBIP10. Under proteasome impairment conditions, interacts with UBD via its histone deacetylase 1 and UBP-type zinc-finger regions. Interacts with CYLD. Interacts with ZMYND15. Belongs to the histone deacetylase family. HD type 2 subfamily.

Protein type: Nuclear receptor co-regulator; EC 3.5.1.98; Ubiquitin conjugating system; Deacetylase

Chromosomal Location of Human Ortholog: Xp11.23

Cellular Component: microtubule; dendrite; histone deacetylase complex; leading edge; perikaryon; caveola; inclusion body; cytosol; nucleoplasm; dynein complex; microtubule associated complex; cytoplasmic microtubule; axon; perinuclear region of cytoplasm; cytoplasm; nucleus

Molecular Function: zinc ion binding; histone deacetylase binding; microtubule binding; beta-tubulin binding; beta-catenin binding; misfolded protein binding; Hsp90 protein binding; actin binding; protein binding; NAD-dependent histone deacetylase activity (H3-K9 specific); enzyme binding; NAD-dependent histone deacetylase activity (H3-K14 specific); tubulin deacetylase activity; ubiquitin protein ligase binding; NAD-dependent histone deacetylase activity (H4-K16 specific); histone deacetylase activity; polyubiquitin binding; tau protein binding; alpha-tubulin binding

Biological Process: negative regulation of proteolysis; response to misfolded protein; protein polyubiquitination; ubiquitin-dependent protein catabolic process via the multivesicular body pathway; positive regulation of signal transduction; transcription, DNA-dependent; regulation of fat cell differentiation; negative regulation of microtubule depolymerization; macroautophagy; organelle organization and biogenesis; response to toxin; misfolded or incompletely synthesized protein catabolic process; histone deacetylation; regulation of gene expression, epigenetic; response to organic substance; intracellular protein transport; protein complex disassembly; protein amino acid deacetylation; lysosome localization; negative regulation of oxidoreductase activity; regulation of receptor activity; negative regulation of transcription, DNA-dependent; negative regulation of protein complex disassembly

Disease: Chondrodysplasia With Platyspondyly, Distinctive Brachydactyly, Hydrocephaly, And Microphthalmia

Research Articles on HDAC6

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Product Notes

The HDAC6 hdac6 (Catalog #AAA388216) is a Recombinant Protein produced from Baculovirus and is intended for research purposes only. The product is available for immediate purchase. It is sometimes possible for the material contained within the vial of "HDAC6, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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